Phosphoproteomics Reveals the AMPK Substrate Network in Response to DNA Damage and Histone Acetylation.

AMP-activated protein kinase (AMPK) is a conserved energy sensor that plays roles in diverse biological processes via phosphorylating various substrates. Emerging studies have demonstrated the regulatory roles of AMPK in DNA repair, but the underlying mechanisms remain to be fully understood. Herein, using mass spectrometry-based proteomic technologies, we systematically investigate the regulatory network of AMPK in DNA damage response (DDR).

AMPK-mediated phosphorylation on 53BP1 promotes c-NHEJ.

AMP-activated protein kinase (AMPK) is an energy sensor that plays roles in multiple biological processes beyond metabolism. Several studies have suggested that AMPK is involved in the DNA damage response (DDR), but the mechanisms remain unclear. Herein, we demonstrate that AMPK promotes classic non-homologous end joining (c-NHEJ) in double-strand break (DSB) repair through recruiting a key chromatin-based mediator named p53-binding protein 1 (53BP1), which facilitates the end joining of distal DNA ends during DDR.

An ultrasensitive fluorogenic probe for revealing the role of glutathione in chemotherapy resistance.

Unveiling the detailed roles of glutathione (GSH) in chemoresistance necessitates a reliable assay for its detection in intact live specimens. Herein, by taking advantage of the susceptibility of electron-poor C -S bond to GSH nucleophilic attack, we developed a naphthalimide-sulfoxide based fluorogenic probe () applicable for tracking endogenous GSH fluctuation in live cells. features a high degree of sensitivity towards GSH as demonstrated by its utmost 2200-fold fluorogenic response.